1FO0

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.218 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule.

Reiser, J.B.Darnault, C.Guimezanes, A.Gregoire, C.Mosser, T.Schmitt-Verhulst, A.-M.Fontecilla-Camps, J.C.Malissen, B.Housset, D.Mazza, G.

(2000) Nat Immunol 1: 291-297

  • DOI: https://doi.org/10.1038/79728
  • Primary Citation of Related Structures:  
    1FO0

  • PubMed Abstract: 

    Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.


  • Organizational Affiliation

    Laboratoire de Cristallographie et Cristallogénèse des Protéines, Institut de Biologie Structurale J.-P. Ebel, CEA-CNRS-UJF, 41, rue Jules Horowitz, F-38027 Grenoble, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (ALLOGENEIC H-2KB MHC CLASS I MOLECULE)A [auth H]276Mus musculusMutation(s): 0 
UniProt
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UniProt GroupP01901
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (BETA-2 MICROGLOBULIN)B [auth L]99Mus musculusMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P01887 (Mus musculus)
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IMPC:  MGI:88127
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
NATURALLY PROCESSED OCTAPEPTIDE PBM1C [auth P]8N/AMutation(s): 0 
UniProt
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UniProt GroupQ8CDD8
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (BM3.3 T CELL RECEPTOR ALPHA-CHAIN)D [auth A]116Mus musculusMutation(s): 0 
UniProt
Find proteins for Q5R1F1 (Mus musculus)
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UniProt GroupQ5R1F1
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (BM3.3 T CELL RECEPTOR BETA-CHAIN)E [auth B]112Mus musculusMutation(s): 0 
UniProt
Find proteins for P04214 (Mus musculus)
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UniProt GroupP04214
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.218 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.58α = 90
b = 120.42β = 90
c = 102.85γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
REFMACrefinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2000-10-02
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-02-01
    Changes: Database references, Structure summary
  • Version 1.4: 2023-08-09
    Changes: Data collection, Database references, Refinement description